A novel phenol hydroxylase and catechol 2,3-dioxygenase from the thermophilic Bacillus thermoleovorans strain A2: Nucleotide sequence and analysis of the genes

FEMS Microbiology Letters

Volumn 161, Issue 1, 1998, Pages 37-45

  Duffner, Fiona M ^a,b   Müller, Rudolf ^a  

^a HAMBURG UNIVERSITY OF TECHNOLOGY   (Germany)

^b NOVO NORDISK A S   (Denmark)

Author keywords

Bacillus thermoleovorans; Catechol 2,3 dioxygenase; Phenol hydroxylase; Thermophile

Indexed keywords

CATECHOL 2,3 DIOXYGENASE; MONOPHENOL MONOOXYGENASE; OXYGENASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACILLUS; BACTERIAL METABOLISM; DRUG DEGRADATION; ENZYME ACTIVITY; GENE INSERTION; MOLECULAR CLONING; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; THERMOPHILIC BACTERIUM;

BACILLUS; CATECHOL 2,3-DIOXYGENASE; CLONING, MOLECULAR; DIOXYGENASES; GENES, BACTERIAL; MIXED FUNCTION OXYGENASES; OXYGENASES;

EID: 0032053780     PISSN: 03781097     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1097(98)00047-0     Document Type: Article

References (25)

1. Berquist, P.L., Love, D.R., Croft, J.E., Streiff, M.B., Daniel, R.M. and Morgan, W.H. (1987) Genetics and potential biotechnological applications of thermophilic and extremely thermophilic microorganisms. Biotechnol. Genet. Eng. Rev. 5, 199-244.
2. Adams, D. and Ribbons, D.W. (1988) The metabolism of aromatic compounds by thermophilic bacilli. Appl. Biochem. Biotechnol. 17, 231-244.
3. Buswell, J.A. and Twomey, G. (1975) Utilization of phenol and cresols by Bacillus stearothermophilus, strain PH24. J. Gen. Microbiol. 87, 377-379.
4. Gurujeyalakshmi, G. and Oriel, P. (1989) Isolation of phenol-degrading Bacillus stearothermophilus and partial characterisation of the phenol hydroxylase. Appl. Environ. Microbiol. 55, 500-502.
5. Kim, I.C. and Oriel, P.J. (1995) Characterization of the Bacillus stearothermophilus BR219 phenol hydroxylase gene. Appl. Environ. Microbiol. 61, 1252-1256.
6. Dong, F.-M., Wang, L.-L., Wang, C.-M., Cheng, J.-P., He, Z.-Q., Sheng, Z.-J. and Shen, R.-Q. (1992) Molecular cloning and mapping of phenol degradation genes from Bacillus stearothermophilus FDTP-3 and their expression in Escherichia coli. Appl. Environ. Microbiol. 58, 2531-2535.
7. Mutzel, A., Reinscheid, U.M., Antranikian, G. and Müller, R. (1996) Isolation and characterization of a thermophilic bacillus strain, which degrades phenol and cresols as sole carbon source at 70°C. Appl. Microbiol. Biotechnol. 46, 593-596.
8. Sambrook, J., Fritsch, E. and Maniatis, T. (1989) Molecular Cloning: A Laboratory Manual, 2nd edn. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
9. Yanisch-Perron, C., Vieira, J. and Messing, J. (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33, 103-109.
10. Inoue, H., Nojima, H. and Okayama, H. (1990) High efficiency transformation of Escherichia coli with plasmids. Gene 96, 23-28.
11. Schägger, H. and van Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379.
12. Altschul, S.F., Gish, W., Miller, W., Myers, E.W. and Lipman, D.L. (1990) Basic local alignment search tool. J. Mol. Biol. 215, 403-410.
13. Thompson, J.D., Higgins, D.G. and Gibson, T.J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680.
14. Kukor, J.J and Olsen, R.H. (1992) Complete nucleotide sequence of tbuD, the gene encoding phenol/cresol hydroxylase from Pseudomonas pickettii PKO1, and functional analysis of the encoded enzyme. J. Bacteriol. 174, 6518-6526.
15. Prieto, M.A. and Garcia, J.L. (1994) Molecular characterisation of 4-hydroxyphenylacetate 3-hydroxylase of Escherichia coli. A two-protein component system. J. Biol. Chem. 269, 22823-22829.
16. Gibello, A., Suarez, M., Allende, J.L. and Martin, M. (1997) Molecular cloning and analysis of the genes encoding the 4-hydroxyphenylacetate hydroxylase from Klebsiella pneumoniae. Arch. Microbiol. 167, 160-166.
17. Takizawa, N., Yokoyama, H., Yanagihara, K., Hatta, T. and Kiyohara, H. (1995) A locus of Pseudomonas pickettii DTP0602 had, that encodes 2,4,6-trichlorophenol-4-dechlorinase with hydroxylase activity and hydroxylation of various chlorophenols by the enzyme. J. Ferment. Bioeng. 80, 318-326.
18. Wierenga, R.K., Terpstra, P. and Hol, W.G.J. (1986) Prediction of the occurrence of the ADP-binding βaβ-fold in proteins using an amino acid sequence fingerprint. J. Mol. Biol. 187, 101-107.
19. Eggink, G., Engel, H., Vriend, G., Terpstra, P. and Witholt, B. (1990) Rubredoxin reductase of Pseudomonas oleovorans. Structural relationship to other flavoprotein oxidoreductases based on one NAD and two FAD fingerprints. J. Mol. Biol. 212, 135-142.
20. Milo, R., Duffner, F., Bauer, M. and Mueller, R. (1997) Degradation of phenol by thermophilic Bacillus species, purification and characterisation of the catechol 2, 3-dioxygenase. In: 8th European Congress on Biotechnology Book of Abstracts, Hungarian Biochemical Society 8, p. 39.
21. Kukor, J.J. and Olsen, R.H. (1996) Catechol 2,3-dioxygenases functional in oxygen limited (hypoxic) environments. Appl. Environ. Microbiol. 62, 1728-1740.
22. Prieto, M.A., Diaz, E. and Garcia, J.L. (1996) Molecular characterization of the 4-hydroxyphenylacetate catabolic pathway of Escherichia coli W: engineering a mobile aromatic degradative cluster. J. Bacteriol. 178, 111-120.
23. Roper, D.I. and Cooper, R.A. (1990) Subcloning and nucleotide sequence of the 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase gene from Escherichia coli C. FEBS Lett. 275, 53-57.
24. Eltis, L.D. and Bolin, J.T. (1996) Evolutionary relationships among extradiol dioxygenases. J. Bacteriol. 178, 5930-5937.
25. Han, S., Eltis, L.D., Timmis, K.N., Muchmore, S.W. and Bolin, J.T. (1995) Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading pseudomonad. Science 270, 976-980.